Team:Bordeaux/Parts/BBa K1317003

From 2014.igem.org

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Link to the registry of Standard Parts: [http://parts.igem.org/Part:BBa_K1317003 http://parts.igem.org/Part:BBa_K1317003]
Link to the registry of Standard Parts: [http://parts.igem.org/Part:BBa_K1317003 http://parts.igem.org/Part:BBa_K1317003]
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===References===
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[1] Doreen M. Floss et al. ''ELASTIN-like polypeptides revolutionize recombinant protein expression and their biomedical application.'' Trends in Biotechnology Vol.28 No.1 (PMID 19897265)
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[2] Dan W. Urry ''Entropic Elastic Processes in Protein Mechanisms. I. Elastic Structure Due to an Inverse Temperature Transition and Elasticity Due to Internal Chain Dynamics.'' Journal of Protein Chemistry, Vol. 7, No.. I, 1988
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[3] Dan W. Urry. Physical ''Chemistry of Biological Free Energy Transduction As Demonstrated by Elastic Protein-Based Polymers.'' J. Phys. Chem. B 1997, 101, 11007-11028
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[4] Dan E. Meyer and Ashutosh Chilkoti. ''Purification of recombinant proteins by fusion with thermally-responsive polypeptides.'' NATURE BIOTECHNOLOGY VOL 17 NOVEMBER 1999
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[5] Trabbic-Carlson et al. (2004), ''Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion.'' Protein Science, 13: 3274–3284. doi: 10.1110/ps.04931604
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[6] K. Trabbic‐Carlson et al. ''Effect of protein fusion on the transition temperature of an environmentally responsive elastin‐like polypeptide: a role for surface hydrophobicity?'' Protein Engineering, Design and Selection (2004) 17 (1): 57-66. doi: 10.1093/protein/gzh006
{{:Team:Bordeaux/Pied}}
{{:Team:Bordeaux/Pied}}

Revision as of 17:26, 17 October 2014

Link to the registry of Standard Parts: [http://parts.igem.org/Part:BBa_K1317003 http://parts.igem.org/Part:BBa_K1317003]

References

[1] Doreen M. Floss et al. ELASTIN-like polypeptides revolutionize recombinant protein expression and their biomedical application. Trends in Biotechnology Vol.28 No.1 (PMID 19897265)

[2] Dan W. Urry Entropic Elastic Processes in Protein Mechanisms. I. Elastic Structure Due to an Inverse Temperature Transition and Elasticity Due to Internal Chain Dynamics. Journal of Protein Chemistry, Vol. 7, No.. I, 1988

[3] Dan W. Urry. Physical Chemistry of Biological Free Energy Transduction As Demonstrated by Elastic Protein-Based Polymers. J. Phys. Chem. B 1997, 101, 11007-11028

[4] Dan E. Meyer and Ashutosh Chilkoti. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. NATURE BIOTECHNOLOGY VOL 17 NOVEMBER 1999

[5] Trabbic-Carlson et al. (2004), Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion. Protein Science, 13: 3274–3284. doi: 10.1110/ps.04931604

[6] K. Trabbic‐Carlson et al. Effect of protein fusion on the transition temperature of an environmentally responsive elastin‐like polypeptide: a role for surface hydrophobicity? Protein Engineering, Design and Selection (2004) 17 (1): 57-66. doi: 10.1093/protein/gzh006

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